Hydrophobic interaction chromatography (HIC) media interact with hydrophobic regions present on an antibody of interest and the characteristics of that interaction can be calibrated by selecting specific HIC media types and binding conditions. In the context of commercial chromatographic purification, HIC medias are used to separate antibody product present in a variety of sample mixtures, including partially purified samples, e.g., samples that have been subjected to filtration and/or one or more step of affinity, ion exchange, and/or mixed mode chromatography. HIC is conventionally used in such strategies as a means for retaining an antibody product on a chromatographic support, while allowing other components in a partially purified sample, including product-related substances (e.g., product aggregates and fragments) and process-related impurities (e.g., host cell proteins), to be washed from the support and discarded and/or allow for the impurities to be resolved from the antibody product by selective elution of the antibody product. The retained antibody product can then be eluted from the chromatographic support by disrupting the antibody/HIC media interaction and the product can subsequently be subjected to further purification steps, e.g., those relying on charge (e.g., ion exchange chromatography), biological interaction characteristics (e.g., affinity chromatography), and/or size (e.g., ultrafiltration).
There remains a need in the art for high-efficiency methods of purifying antibody products away from product-related substances and process-related impurities at relatively low cost. Reduction of such substances and/or impurities is particularly advantageous in the context of commercially produced recombinant bio-therapeutics as such substances and/or impurities have the potential to impact numerous product characteristics, including, but not limited to, product stability, product safety and product efficacy.